3L26_OPHHA
ID 3L26_OPHHA Reviewed; 91 AA.
AC P82662; Q53B60;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Alpha-elapitoxin-Oh2b;
DE Short=Alpha-EPTX-Oh2b;
DE AltName: Full=Alpha-neurotoxin;
DE AltName: Full=LNTX3;
DE AltName: Full=Long neurotoxin OH-6A/OH-6B;
DE AltName: Full=OH-3;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-33, AND TOXIC DOSE.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15302536; DOI=10.1016/j.toxicon.2004.06.003;
RA He Y.-Y., Lee W.-H., Zhang Y.;
RT "Cloning and purification of alpha-neurotoxins from king cobra (Ophiophagus
RT hannah).";
RL Toxicon 44:295-303(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TOXIC DOSE.
RC TISSUE=Venom gland;
RX PubMed=16689684; DOI=10.1042/bj20060004;
RA Li J., Zhang H., Liu J., Xu K.;
RT "Novel genes encoding six kinds of three-finger toxins in Ophiophagus
RT hannah (king cobra) and function characterization of two recombinant long-
RT chain neurotoxins.";
RL Biochem. J. 398:233-242(2006).
RN [3]
RP PROTEIN SEQUENCE OF 22-91, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=9920740; DOI=10.1006/bbrc.1998.9888;
RA Lin S.-R., Chang L.-S., Chang C.-C.;
RT "Disulfide isomers of alpha-neurotoxins from King cobra (Ophiophagus
RT hannah) venom.";
RL Biochem. Biophys. Res. Commun. 254:104-108(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1) and
CC neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and
CC inhibits acetylcholine from binding to the receptor, thereby impairing
CC neuromuscular and neuronal transmission (By similarity). Recombinant
CC LNTX1 leads to a functional block of the muscle-type acetylcholine
CC receptors. Has a cytotoxic activity. This neurotoxin is lethal
CC (PubMed:16689684). {ECO:0000250|UniProtKB:P60615,
CC ECO:0000269|PubMed:16689684}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9920740}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 0.41 mg/kg by intravenous injection into mice.
CC -!- TOXIC DOSE: LD(50) is 100 ug/kg by intraperitoneal injection into mice.
CC -!- MISCELLANEOUS: OH-6A and OH-6B are disulfide isomers which arise from
CC cis-trans isomerization of the Cys-47-Cys-51 disulfide bond. They
CC differ in the retention time in reversed-phase column and the
CC conformation.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR EMBL; AY596926; AAT97248.1; -; mRNA.
DR EMBL; DQ273568; ABB83622.1; -; mRNA.
DR PIR; JG0189; JG0189.
DR AlphaFoldDB; P82662; -.
DR SMR; P82662; -.
DR TopDownProteomics; P82662; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15302536,
FT ECO:0000269|PubMed:9920740"
FT CHAIN 22..91
FT /note="Alpha-elapitoxin-Oh2b"
FT /id="PRO_0000093561"
FT DISULFID 24..41
FT /evidence="ECO:0000250"
FT DISULFID 34..62
FT /evidence="ECO:0000250"
FT DISULFID 47..51
FT /evidence="ECO:0000250"
FT DISULFID 66..77
FT /evidence="ECO:0000250"
FT DISULFID 78..83
FT /evidence="ECO:0000250"
SQ SEQUENCE 91 AA; 9857 MW; 756AFC1424E97250 CRC64;
MKTLLLTLVV MTIVCLDLGY TLICFISSHD SVTCAPGENV CFLKSWCDAW CGSRGKKLSF
GCAATCPKVN PGIDIECCST DNCNPHPKLR P
